SAXSdb — 1zw0

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1. Protein Identity and Related Structures Protein Identity & Related Structures

type III secretion protein

Yersinia pestis

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	water × 2	Consistent with protein count
10	Protein homooligomer	Homooligomer	Protein 6	water × 6	Consistent with protein count
11	Protein homooligomer	Homooligomer	Protein 6	water × 6	Consistent with protein count
12	Protein homooligomer	Homooligomer	Protein 6	water × 6	Consistent with protein count
13	Protein homooligomer	Homooligomer	Protein 6	water × 6	Consistent with protein count
14	Protein homooligomer	Homooligomer	Protein 4	water × 4	Consistent with protein count
15	Protein homooligomer	Homooligomer	Protein 4	water × 4	Consistent with protein count
2	Protein homooligomer	Homooligomer	Protein 2	water × 2	Consistent with protein count
3	Protein homooligomer	Homooligomer	Protein 2	water × 2	Consistent with protein count
4	Protein homooligomer	Homooligomer	Protein 2	water × 2	Consistent with protein count
5	Protein homooligomer	Homooligomer	Protein 16	water × 16	Consistent with protein count
6	Protein homooligomer	Homooligomer	Protein 16	water × 16	Consistent with protein count
7	Protein homooligomer	Homooligomer	Protein 8	water × 8	Consistent with protein count
8	Protein homooligomer	Homooligomer	Protein 8	water × 8	Consistent with protein count
9	Protein homooligomer	Homooligomer	Protein 8	water × 8	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q7ARI1_YERPE
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–66； UniProt 1–66 Author chain B； PDBConstruct 1–66； UniProt 1–66 Author chain C； PDBConstruct 1–66； UniProt 1–66 Author chain D； PDBConstruct 1–66； UniProt 1–66 Author chain E； PDBConstruct 1–66； UniProt 1–66 Author chain F； PDBConstruct 1–66； UniProt 1–66 Author chain G； PDBConstruct 1–66； UniProt 1–66 Author chain H； PDBConstruct 1–66； UniProt 1–66

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1zw0
Deposition date deposition_date	2005-06-03
Structure title title	Crystal structure of the Yersinia Type III Secretion protein YscE
Keywords keywords	Type III secretion, chaperone, Yersinia, translocation, export; CHAPERONE
Experimental Method method	X-RAY DIFFRACTION

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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

1zw0__assembly_12__model_1

Assembly 12 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1zw0__assembly_12__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1zw0__assembly_12__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	27.74 Å
Rg (electron density)	27.81 Å
Total Rg	28.18 Å
Atom count	2833
Residues	361
Excluded volume	50978 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1zw0__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1zw0__assembly_2__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`1zw0__assembly_3__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
4	1	`1zw0__assembly_4__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
5	1	`1zw0__assembly_5__model_1`	hexadecameric （16）	Success	4.1.3-1-20251215 (887e7ef)	View Download
6	1	`1zw0__assembly_6__model_1`	hexadecameric （16）	Success	4.1.3-1-20251215 (887e7ef)	View Download
7	1	`1zw0__assembly_7__model_1`	octameric （8）	Success	4.1.3-1-20251215 (887e7ef)	View Download
8	1	`1zw0__assembly_8__model_1`	octameric （8）	Success	4.1.3-1-20251215 (887e7ef)	View Download
9	1	`1zw0__assembly_9__model_1`	octameric （8）	Success	4.1.3-1-20251215 (887e7ef)	View Download
10	1	`1zw0__assembly_10__model_1`	hexameric （6）	Success	4.1.3-1-20251215 (887e7ef)	View Download
11	1	`1zw0__assembly_11__model_1`	hexameric （6）	Success	4.1.3-1-20251215 (887e7ef)	View Download
12	1	`1zw0__assembly_12__model_1`	hexameric （6）	Success	4.1.3-1-20251215 (887e7ef)	View Download
13	1	`1zw0__assembly_13__model_1`	hexameric （6）	Success	4.1.3-1-20251215 (887e7ef)	View Download
14	1	`1zw0__assembly_14__model_1`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download
15	1	`1zw0__assembly_15__model_1`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (2)

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6. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

Domain ID domain_id	1zw0A00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	420 — Immunoglobulin FC, subunit C

Domain ID domain_id	1zw0B00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	420 — Immunoglobulin FC, subunit C

Domain ID domain_id	1zw0C00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	420 — Immunoglobulin FC, subunit C

Domain ID domain_id	1zw0D00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	420 — Immunoglobulin FC, subunit C

Domain ID domain_id	1zw0E00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	420 — Immunoglobulin FC, subunit C

Domain ID domain_id	1zw0F00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	420 — Immunoglobulin FC, subunit C

Domain ID domain_id	1zw0G00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	420 — Immunoglobulin FC, subunit C

Domain ID domain_id	1zw0H00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	420 — Immunoglobulin FC, subunit C

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Unit-cell length a length_a	82.969 Å
Unit-cell length b length_b	84.622 Å
Unit-cell length c length_c	81.799 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	32

Space group space_group	P 21 21 2
Space-group number int_tables_number	18
Crystal system crystal_system	—

Resolution resolution	1.800 Å
Low-resolution limit resolution_low	25.000 Å
R factor r_factor	0.2271
R_work r_work	0.2255
R_free r_free	0.2591

Description description	type III secretion protein
Molecular weight formula_weight	7616.9 kDa
Source method src_method	man
Copy count entity_count	8

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H
Atom count atom_count	4104

Crystal structure of the Yersinia Type III Secretion protein YscE

1. Protein Identity and Related Structures Protein Identity & Related Structures

type III secretion protein

State in the Current Structure

Other States of the Same Protein in the Database

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

1zw0__assembly_12__model_1

1zw0__assembly_12__model_1 | I(q)

1zw0__assembly_12__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

7. Citations (1)

Source organism organism	Yersinia pestis
NCBI taxonomy ID ncbi_taxonomy_id	632
Host organism host_organism	Escherichia coli

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	334

Crystal structure of the Yersinia Type III Secretion protein YscE

1. Protein Identity and Related Structures Protein Identity & Related Structures

type III secretion protein

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

1zw0__assembly_12__model_1

1zw0__assembly_12__model_1 | I(q)

1zw0__assembly_12__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

7. Citations (1)